Fig. S1 Hinge analysis.We identified hinge regions in selected structural models with ancient FF domain structures using FlexOracle.Three-dimensional diagrams of the structural space of helical (large cylinders) and strand (small cylinders) regions surrounding the active site (sphere) in the left illustrate the creation of bent structures acting as ligand pockets. Structures in the right identify hinge regions with flexibility measured by intra-potential energies for hinge-dissected fragments and described with colors ranging from blue (low) to red (high). A. ATP-binding subunit of the histidine permease from Salmonella typhimurium (1B0U) harboring the ABC transporter ATPase domain-like FF (c.37.1.12; ndFF = 0). B. Class II aaRS homologue (BII0957) complexed with ATP (3MEY) harboring the catalytic domainof class II aaRS-likeFF (d.104.1.1; ndFF = 0.024). C. Oligo-peptide binding protein (OPPA) complexed with KAK (1JET) harboring the phosphate binding protein-like FF (c.94.1.1; ndFF = 0.033). D. Phenylalanine activating domain of gramicidin synthetase 1 in a complex with AMP and phenylalanine (1AMU) harboring the acetyl-CoA synthetase-like FF (e.23.1.1; ndFF = 0.045). Note that 90.7% and 92% of the structures in A and B are rigid, respectively, suggesting there is no true hinge regions in these proteins
Fig. S2 The evolutionary appearance of protein cofactors based on COGNATE and non-COGNATE associations. The heatmap shows the quantitative association of cofactors with ancient FFs based on relationships that exist between cofactors and FFs from thePROCOGNATE and the PDB databasesThe COGNATE dataset contains only experimentally verified relationships and the non-COGNATE dataset includes relationships that are not validated experimentally. The 54 most ancient FFs are arranged by their nd values (e.g., the most ancient FF = c.37.1.12; the most recent FF = d.14.1.1). Cofactors are ordered according to their first time appearances in the timeline according to thend values of the FFs (left: appearing earlier; right: appearing later). The values in cells indicate the numbers of PDB chains of FFs bound to the cofactors, normalized to a scale 0 to 1, and are visualized in a scale of color intensity.Stronger associations between a cofactor and its FF have hues that are closer to red. The complete absence of the association is labeled in gray
Table S1 The 54 most ancient FFs
FF ccs / FF name / F name / F structure / FSF structure / FF structurec.37.1.12 / ABC transporter ATPase domain-like / P-loop containing nucleoside triphosphate hydrolases / 3 layers: , parallel or mixed -sheets of variable sizes / Division into families based on -sheet topologies / There are two additional subdomains inserted into the central core that has a RecA-like topology
c.37.1.20 / Extended AAA-ATPase domain / P-loop containing nucleoside triphosphate hydrolases / 3 layers: , parallel or mixed -sheets of variable sizes / Division into families based on -sheet topologies / Fold is similar to that of RecA, but lacks the last two strands, followed by a FF-specific Arg-finger domain
c.2.1.2 / Tyrosine-dependent oxidoreductases / NAD(P)-binding Rossmann-fold domains / Core: 3 layers, , parallel sheet of 6 strands, order 321456
The nucleotide-binding modes of this and the next two F/FSFs are similar / - / Also known as short-chain dehydrogenases and SDR family parallel sheet is extended by 7th strand, order 3214567; left-handed crossover connection between strands 6 and 7
c.37.1.19 / Tandem AAA-ATPase domain / P-loop containing nucleoside triphosphate hydrolases / 3 layers: , parallel or mixed sheets of variable sizes / Division into families based on sheet topologies / Duplication: tandem repeat of two RecA-like (AAA) domains
c.55.1.1 / Actin/HSP70 / Ribonuclease H-like motif / 3 layers: , mixed sheetof 5 strands, order 32145; strand 2 is antiparallel to the rest / Duplication contains two domains of this fold / -
c.37.1.8 / G proteins / P-loop containing nucleoside triphosphate hydrolases / 3 layers: , parallel or mixed sheets of variable sizes / Division into families based on sheet topologies / Core: mixedsheet of 6 strands, order 231456; strand 2 is antiparallel to the rest
c.26.1.1 / Class I aminoacyl-tRNA synthetases (RS), catalytic domain / Adenine nucleotide alpha hydrolase-like / Core: 3 layers, , parallel sheetof 5 strands, order 32145 / - / Contains a conserved all subdomain at the C-terminal extension
d.104.1.1 / Class II aminoacyl-tRNA synthetase (aaRS)-like, catalytic domain / Class II aaRS and biotin synthetases / Contains large mixed sheet / - / -
c.67.1.4 / GABA-aminotransferase-like / PLP-dependent transferase-like / Main domain: 3 layers: , mixed sheetof 7 strands, order 3245671; strand 7 is antiparallel to the rest / - / Formerly omega-aminoacid:pyruvate aminotransferase-like
c.94.1.1 / Phosphate binding protein-like / Periplasmic binding protein-like II / Consists of two similar intertwined domain with 3 layers () each: duplication mixed sheet of 5 strands, order 21354; strand 5 is antiparallel to the rest / Similar in architecture to the FSF I but partly differs in topology / -
c.95.1.1 / Thiolase-related / Thiolase-like / Consists of two similar domains related by pseudo dyad, duplication; 3 layers: ; mixed sheetof 5 strands, order 32451; strand 5 is antiparallel to the rest / - / -
c.1.4.1 / FMN-linked oxidoreductases / TIM beta/alpha-barrel / Contains parallel sheet barrel, closed; n=8, S=8; strand order 12345678; the first seven FSF have similar phosphate-binding sites / - / -
c.37.1.11 / RecA protein-like (ATPase-domain) / P-loop containing nucleoside triphosphate hydrolases / 3 layers: , parallel or mixed sheets of variable sizes / Division into FFs based on sheet topologies / Core: mixed sheetof 8 strands, order 32451678; strand 7 is antiparallel to the rest
e.23.1.1 / Acetyl-CoA synthetase-like / Acetyl-CoA synthetase-like / 4 domains: (1&2) duplication: share the same fold; (3) -barrel; (4) / - / -
c.82.1.1 / ALDH-like / ALDH-like / Consists of two similar domains with 3 layers () each, duplication; core: parallel sheetof 5 strands, order 32145 / Binds NAD differently from other NAD(P)-dependent oxidoreductases / -
c.79.1.1 / Tryptophan synthase beta subunit-like PLP-dependent enzymes / Tryptophan synthase beta subunit-like PLP-dependent enzymes / Consists of two similar domains related by pseudo dyad, duplication; core: 3 layers, ; parallel sheetof 4 strands, order 3214 / - / -
c.67.1.3 / Cystathionine synthase-like / PLP-dependent transferase-like / Main domain: 3 layers: , mixed sheetof 7 strands, order 3245671; strand 7 is antiparallel to the rest / - / -
c.37.1.10 / Nitrogenase iron protein-like / P-loop containing nucleoside triphosphate hydrolases / 3 layers: , parallel or mixed sheets of variable sizes / Division into FFs based on sheettopologies / Core: parallel sheetof 7 strands; order 3241567
c.23.16.1 / Class I glutamine amidotransferases (GAT) / Flavodoxin-like / 3 layers, ; parallel sheetof 5 strand, order 21345 / Conserved positions of the oxyanion hole and catalytic nucleophile; different constituent FFs contain different additional structures / Contains a catalytic Cys-His-Glu triad
c.67.1.1 / AAT-like / PLP-dependent transferase-like / Main domain: 3 layers: , mixed sheetof 7 strands, order 3245671; strand 7 is antiparallel to the rest / - / -
d.142.1.2 / BC ATP-binding domain-like / ATP-grasp / Consists of two subdomains with different folds; shares functional and structural similarities with the PIPK and protein kinase FSFs / - / -
c.30.1.1 / BC N-terminal domain-like / PreATP-grasp domain / 3 layers: ; parallel or mixed sheetof 4 to 6 strands possible rudiment form of Rossmann-fold domain / Precedes the ATP-grasp domain common to all FSF members, can contain a substrate-binding function / -
c.2.1.7 / Aminoacid dehydrogenase-like, C-terminal domain / NAD(P)-binding Rossmann-fold domains / Core: 3 layers, ; parallel sheetof 6 strands, order 321456; the nucleotide-binding modes of this and the next two F/FSFs are similar / - / Extra N-terminal helix displaces the C-terminal helix (following strand 6) from its usual position creating a family nicotinamide-binding site
c.61.1.1 / Phosphoribosyltransferases (PRTases) / PRTase-like / Core: 3 layers, ; mixed sheetof 6 strands, order 321456; strand 3 is antiparallel to the rest / - / -
c.37.1.1 / Nucleotide and nucleoside kinases / P-loop containing nucleoside triphosphate hydrolases / 3 layers: , parallel or mixed sheets of variable sizes / Division into families based on beta-sheet topologies / Parallel sheetof 5 strands, order 23145
b.43.3.1 / Elongation factors / Reductase/isomerase/elongation factor common domain / Barrel, closed; n=6, S=10; greek-key / - / -
c.1.8.1 / Amylase, catalytic domain / TIM beta/alpha-barrel / Contains parallel sheetbarrel, closed; n=8, S=8; strand order 12345678; the first seven FSFs have similar phosphate-binding sites / - / Members of the family may contain various insert subdomains in -amylases and closer relatives this domain is usually followed by a common all- domain
d.127.1.1 / Creatinase/aminopeptidase / Creatinase/aminopeptidase / Duplication: composed of two very similar folds / - / -
c.1.7.1 / Aldo-keto reductases (NADP) / TIM beta/alpha-barrel / Contains parallel sheet barrel, closed; n=8, S=8; strand order 12345678; the first seven FSFs have similar phosphate-binding sites / - / Common fold covers whole protein structure
d.153.1.1 / Class II glutamine amidotransferases / Ntn hydrolase-like / 4 layers: ; has an unusual sheet-to-sheet packing / N-terminal residue provides two catalytic groups, nucleophile and proton donor / Has slightly different topology than other FFs
c.1.10.1 / Class I aldolase / TIM beta/alpha-barrel / Contains parallel sheet barrel, closed; n=8, S=8; strand order 12345678; the first seven FSFs have similar phosphate-binding sites / Common fold covers whole protein structure / The catalytic lysine forms schiff-base intermediate with substrate possible link between the aldolase FSF and the phosphate-binding barrels
c.2.1.4 / Formate/glycerate dehydrogenases, NAD-domain / NAD(P)-binding Rossmann-fold domains / Core: 3 layers, ; parallel beta-sheet of 6 strands, order 321456
The nucleotide-binding modes of this and the next two F/FSFs are similar / - / This domain interrupts the other domain which defines the FF
a.127.1.1 / L-aspartase/fumarase / L-aspartase-like / Multihelical, consists of three all- domains / - / -
c.78.1.1 / Aspartate/ornithine carbamoyltransferase / ATC-like / Consists of two similar domains related by pseudo dyad, duplication; core: 3 layers, , parallel sheet of 4 strands, order 2134 / - / -
c.26.2.1 / N-type ATP pyrophosphatases / Adenine nucleotide alpha hydrolase-like / Core: 3 layers, , parallel sheet of 5 strands, order 32145 / Share similar mode of ligand (adenosine group) binding can be subdivided into two groups with closer relationships within each group than between the groups; the first 3FFs form one group whereas the last two FFs form the other group / -
c.2.1.6 / 6-phosphogluconate dehydrogenase-like, N-terminal domain / NAD(P)-binding Rossmann-fold domains / Core: 3 layers, , parallel sheet of 6 strands, order 321456; the nucleotide-binding modes of this and the next two F/FSFs are similar / - / The sheet is extended to 8 strands, order 32145678; strands 7 & 8 are antiparallel to the rest; C-terminal domains also show some similarity
c.2.1.3 / Glyceraldehyde-3-phosphate dehydrogenase-like, N-terminal domain / NAD(P)-binding Rossmann-fold domains / Core: 3 layers, , parallel sheet of 6 strands, order 321456; the nucleotide-binding modes of this and the next two F/FSFs are similar / - / FF members also share a common fold in the C-terminal domain
d.81.1.1 / GAPDH-like / FwdE/GAPDH domain-like / Core: (3); mixed sheet: 2134, strand 2 is parallel to strand 1 / N-terminal domain is the classic Rossmann-fold / Has many additional secondary structures
c.83.1.1 / Aconitase iron-sulfur domain / Aconitase iron-sulfur domain / Consists of three similar domains with 3 layers () each, duplication; core: parallel sheet of 5 strands, order 32145 / - / Duplication: consists of 3 structurally similar subdomains with subdomains 1 and 3 being related by pseudo two-fold symmetry
c.77.1.1 / Dimeric isocitrate & isopropylmalate dehydrogenases / Isocitrate/Isopropylmalate dehydrogenase-like / Consists of two intertwined (sub)domains related by pseudo dyad; duplication 3 layers: ; single mixed sheet of 10 strands, order 213A945867 (A=10); strands from 5 to 9 are antiparallel to the rest / The constituent FFs form similar dimers / The active site is between the two identical subunits
d.79.4.1 / PurM N-terminal domain-like / Bacillus chorismate mutase-like / Core: -- (2); mixed sheet: order: 1423, strand 4 is antiparallel to the rest / - / -
d.139.1.1 / PurM C-terminal domain-like / PurM C-terminal domain-like / 3 layers: ; partial topological similarity to the ferredoxin-like fold / - / -
b.40.4.5 / Cold shock DNA-binding domain-like / OB-fold / Barrel, closed or partly opened n=5, S=10 or S=8; greek-key / - / Barrel, closed; n=5, S=8
b.44.1.1 / EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain / Elongation factor/aminomethyltransferase common domain / Barrel, closed; n=6, S=10; greek-key / Probably related to the second domain and its FSF by a circular permutation
c.117.1.1 / Amidase signature (AS) enzymes / Amidase signature (AS) enzymes / Possible duplication: the topologies of N- and C-terminal halves are similar; 3 layers: ; single mixed sheet of 10 strands, order 213549A867 (A=10); strands from 5 to 9 are antiparallel to the rest / - / -
c.2.1.1 / Alcohol dehydrogenase-like, C-terminal domain / NAD(P)-binding Rossmann-fold domains / Core: 3 layers, ; parallel sheet of 6 strands, order 321456; the nucleotide-binding modes of this and the next two F/FSFs are similar / - / N-terminal all- domain defines family
b.35.1.2 / Alcohol dehydrogenase-like, N-terminal domain / GroES-like / Contains barrel, partly opened; n*=4, S*=8; meander / - / C-terminal domain is (classical Rossmann-fold)
d.122.1.2 / DNA gyrase/MutL, N-terminal domain / ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase / 8-stranded mixed sheet; 2 layers: / - / -
d.130.1.1 / S-adenosylmethionine synthetase / S-adenosylmethionine synthetase / Duplication: consists of 3 similar intertwined domains structural repeat: (2)-; two layers, / - / -
e.8.1.1 / DNA polymerase I / DNA/RNA polymerases / Divided into morphological domains including "palm", "thumb" and "fingers"; the catalytic "palm" domain is conserved to all members / "Palm" domain has a ferredoxin-like fold, related to that of an adenylyl cyclase domain / -
b.51.1.1 / ValRS/IleRS/LeuRS editing domain / ValRS/IleRS/LeuRS editing domain / Core: barrel, closed; n=6, S=8; topology is similar to that of the acid proteases barrel / - / Inserted into the catalytic domain
e.29.1.1 / RNA-polymerase beta / beta and beta-prime subunits of DNA dependent RNA-polymerase / Multidomain subunits of complex domain organization / The catalytic site is formed by the association of two double--barrel domains, one from each subunit / -
e.29.1.2 / RNA-polymerase beta-prime / beta and beta-prime subunits of DNA dependent RNA-polymerase / Multidomain subunits of complex domain organization / The catalytic site is formed by the association of two double--barrel domains, one from each subunit / -
d.14.1.1 / Translational machinery components / Ribosomal protein S5 domain 2-like / Core: (3); 2 layers: ; left-handed crossover / - / -
Table S2 Age, forms and 3D sheet topologies of the most ancient FFs
FF ccs / FF name / ndFF / Form / Sheet twist / Sheet curlc.37.1.12 / ABC transporter ATPase domain-like / 0 / I4(2) / 0, 2 (1-2) / 0 (0-1), 1 (1-2)
c.37.1.20 / Extended AAA-ATPase domain / 0.004 / I3(1) / 2 (1-3) / 1 (0-1)
c.2.1.2 / Tyrosine-dependent oxidoreductases / 0.008 / I3(1) / 2 (2-3) / 1 (0-1)
c.37.1.19 / Tandem AAA-ATPase domain / 0.012 / I3(1) / 2 (1-3) / 0 (0-3)
c.55.1.1 / Actin/HSP70 / 0.020 / I3(1) / 2 (1-3) / 0 (0-1)
c.37.1.8 / G proteins / 0.020 / I3(1) / 2 (2-3) / 2 (2-3)
c.26.1.1 / Class I aminoacyl-tRNA synthetases (RS), catalytic domain / 0.020 / I3(1) / 2 (1-3) / 0 (0-1)
d.104.1.1 / Class II aminoacyl-tRNA synthetase (aaRS)-like, catalytic domain / 0.024 / I3(1) / 3 (2-3) / 2 (1-2)
c.67.1.4 / GABA-aminotransferase-like / 0.029 / I3(1) / 3 (2-3) / 0 (0-3)
c.94.1.1 / Phosphate binding protein-like / 0.033 / C3(1) / 2 (1-3) / 3 (0-3)
c.95.1.1 / Thiolase-related / 0.041 / I3(1) / 1 (0-2) / 0 (0-1)
c.1.4.1 / FMN-linked oxidoreductases / 0.041 / O2(1) / 3 (3) / 4 (4)
c.37.1.11 / RecA protein-like (ATPase-domain) / 0.045 / C3(1) / 3 (1-3) / 3 (2-3)
e.23.1.1 / Acetyl-CoA synthetase-like / 0.045 / I3(1),O1(1) / 1 (0-2), 3 (3) / 1 (0-2), 4 (4)
c.82.1.1 / ALDH-like / 0.045 / I3(1) / 2 (2) / 0 (0-1)
c.79.1.1 / Tryptophan synthase beta subunit-like PLP-dependent enzymes / 0.053 / I3(1) / 2 (1-3) / 0 (0)
c.67.1.3 / Cystathionine synthase-like / 0.053 / I3(1) / 3 (1-3) / 2 (0-3)
c.37.1.10 / Nitrogenase iron protein-like / 0.057 / C3(1) / 3 (2-3) / 3 (0-3)
c.23.16.1 / Class I glutamine amidotransferases (GAT) / 0.057 / I3(1) / 3 (1-3) / 0 (1-3)
c.67.1.1 / AAT-like / 0.061 / C3(1) / 2 (2-3) / 3 (2-3)
d.142.1.2 / BC ATP-binding domain-like / 0.061 / I3(1) / 2 (2-3) / 0 (0-3)
c.30.1.1 / BC N-terminal domain-like / 0.061 / I3(1) / 2 (2-3) / 0 (0-3)
c.2.1.7 / Aminoacid dehydrogenase-like, C-terminal domain / 0.069 / I3(1) / 1 (1-3) / 0 (0-3)
c.61.1.1 / Phosphoribosyltransferases (PRTases) / 0.069 / I3(1) / 2 (2-3) / 1 (0-1)
c.37.1.1 / Nucleotide and nucleoside kinases / 0.073 / I3(1) / 1 (1-2) / 1 (0-1)
b.43.3.1 / Elongation factors / 0.073 / O1(1) / 3 (3) / 4 (4)
c.1.8.1 / Amylase, catalytic domain / 0.078 / O2(1) / 3 (3) / 4 (4)
d.127.1.1 / Creatinase/aminopeptidase / 0.078 / C3(1) / 3 (0-3) / 2 (0-4)
c.1.7.1 / Aldo-keto reductases (NADP) / 0.078 / O2(1) / 3 (3) / 4 (4)
d.153.1.1 / Class II glutamine amidotransferases / 0.086 / I4(2) / - / -
c.1.10.1 / Class I aldolase / 0.086 / O2(1) / 3 (3-3) / 4 (4)
c.2.1.4 / Formate/glycerate dehydrogenases, NAD-domain / 0.086 / I3(1) / 2 (1-3) / 0 (0-1)
a.127.1.1 / L-aspartase/fumarase / 0.094 / MOB / - / -
c.78.1.1 / Aspartate/ornithine carbamoyltransferase / 0.098 / I3(1) / 2 (1-3) / 0 (0)
c.26.2.1 / N-type ATP pyrophosphatases / 0.098 / I3(1) / 2 (2-3) / 1 (1)
c.2.1.6 / 6-phosphogluconate dehydrogenase-like, N-terminal domain / 0.098 / I3(1) / 3 (0-3) / 0 (0-3)
c.2.1.3 / Glyceraldehyde-3-phosphate dehydrogenase-like, N-terminal domain / 0.098 / I3(1) / 2 (1-3) / 2 (0-2)
d.81.1.1 / GAPDH-like / 0.098 / I2(1) / 3 (1-3) / 1 (1-2)
c.83.1.1 / Aconitase iron-sulfur domain / 0.106 / I3(1) / 3 (1-3) / 0 (0-1)
c.77.1.1 / Dimeric isocitrate & isopropylmalate dehydrogenases / 0.110 / I3(1) / 3 (3) / 0 (0)
d.79.4.1 / PurM N-terminal domain-like / 0.110 / I2(1) / 3 (1-3) / 0 (1-3)
d.139.1.1 / PurM C-terminal domain-like / 0.110 / I2(1) / 1 (1-3) / 0 (0-3)
b.40.4.5 / Cold shock DNA-binding domain-like / 0.114 / O1(1) / 3 (3) / 4 (3-4)
b.44.1.1 / EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain / 0.114 / O1(1) / 3 (3) / 4 (4)
c.117.1.1 / Amidase signature (AS) enzymes / 0.114 / I3(1) / 3 (3) / 1 (0-1)
c.2.1.1 / Alcohol dehydrogenase-like, C-terminal domain / 0.118 / I3(1) / 2 (1-2) / 0 (0-3)
b.35.1.2 / Alcohol dehydrogenase-like, N-terminal domain / 0.118 / OC1(1) / 2 (2-3) / 4 (4)
d.122.1.2 / DNA gyrase/MutL, N-terminal domain / 0.118 / I2(1) / 1 (0-1) / 1 (1)
d.130.1.1 / S-adenosylmethionine synthetase / 0.122 / I2(1) / 0 (0-1) / 1 (0-2)
e.8.1.1 / DNA polymerase I / 0.122 / I3(1) UDB / 1 (1), 2 (0-2) / 0 (0-1), 1 (0-2)
b.51.1.1 / ValRS/IleRS/LeuRS editing domain / 0.126 / O1(1) / 2 (1-2) / 4 (4)
e.29.1.1 / RNA-polymerase beta / 0.126 / O1(1) CX / 0 (0-1), 4 / 0,1,1
e.29.1.2 / RNA-polymerase beta-prime / 0.126 / O1(1) CX / 2 (0-3), 4 / 0,1,2,4
d.14.1.1 / Translational machinery components / 0.126 / I3(1) O1(1) I2(1) / 1 (1-3), 3 (3) / 1 (1-3), 4 (4)
Sheet twist and curl are defined in materials and methods. MOB, multihelical orthogonal bundle; UDB, up-and-down bundle; CX, complex.
Table S3 Structural matches of the ANBP structure to the 54 most ancient FFs
FF / SCOP protein domain description / Age (ndFF) / SCOP code / % aligned residues / No. aligned residues / RMSD (Å)c.37.1.20 / CDC6-like protein APE0152, N-terminal domain / 0.0041 / d1w5sa2 / 71 / 49 / 3.41
c.37.1.8 / Rab9a / 0.0204 / d1wmsa_ / 72 / 50 / 3.31
d.104.1.1 / Glycyl-tRNA synthetase (GlyRS) / 0.0245 / d1atia2 / 72 / 50 / 2.83
d.104.1.1 / Aspartyl-tRNA synthetase (AspRS) / 0.0245 / d1b8aa2 / 75 / 52 / 3.05
d.104.1.1 / Alanyl-tRNA synthetase (AlaRS) / 0.0245 / d1riqa2 / 71 / 49 / 3.14
d.104.1.1 / Phenyl-tRNA synthetase (PheRS) alpha subunit, PheS / 0.0245 / d1jjca_ / 71 / 49 / 3.29
d.104.1.1 / Histidyl-tRNA synthetase (HisRS) / 0.0245 / d1wu7a2 / 71 / 49 / 3.32
d.139.1.1 / Selenide, water dikinase SelD / 0.1102 / d2zoda2 / 71 / 49 / 3.21
c.117.1.1 / Glutamyl-tRNA(Gln) amidotransferase subunit A / 0.1142 / d2gi3a1 / 73 / 51 / 3.14
c.117.1.1 / Malonamidase E2 / 0.1143 / d1ocka_ / 71 / 49 / 2.94
d.122.1.2 / DNA topoisomerase II / 0.1184 / d1pvga2 / 71 / 49 / 3.01
d.122.1.2 / Topoisomerase IV subunit B / 0.1184 / d1s14a_ / 73 / 51 / 3.25
e.8.1.1 / Family B DNA polymerase / 0.1224 / d1s5ja2 / 71 / 49 / 2.66
d.104.1.1 / Prolyl-tRNA synthetase (ProRS) / 0.1918 / d1hc7a2 / 73 / 51 / 3.00
1